Nicole S. Sampson
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View article: Pharmacologic properties and inhibitory activity of 6-azasteroids against <i>Mycobacterium leprae in vivo</i> and <i>in vitro</i>
Pharmacologic properties and inhibitory activity of 6-azasteroids against <i>Mycobacterium leprae in vivo</i> and <i>in vitro</i> Open
Although the current multidrug therapy (MDT) for leprosy is very successful, the long treatment duration and the emergence of antibiotic-resistant strains demand for new alternative drugs. One potential target for drug development against …
View article: <i>Mycobacterium tuberculosis</i> Mce3R TetR-like Repressor Forms an Asymmetric Four-Helix Bundle and Binds a Nonpalindrome Sequence
<i>Mycobacterium tuberculosis</i> Mce3R TetR-like Repressor Forms an Asymmetric Four-Helix Bundle and Binds a Nonpalindrome Sequence Open
Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, is a major global health concern. TetR family repressors (TFRs) are important for Mtb's adaptation to the human host environment. Our study focuses on one notable Mtb r…
View article: Mycobacterium tuberculosis Mce3R TetR-like Repressor Forms an Asymmetric Four-Helix Bundle and Binds a Non-Palindrome Sequence
Mycobacterium tuberculosis Mce3R TetR-like Repressor Forms an Asymmetric Four-Helix Bundle and Binds a Non-Palindrome Sequence Open
Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, is a major global health concern. TetR family repressors (TFRs) are important for Mtb's adaptation to the human host environment. Our study focuses on one notable Mtb r…
View article: Glycopolymers Prepared by Alternating Ring-Opening Metathesis Polymerization Provide Access to Distinct, Multivalent Structures for the Probing of Biological Activity
Glycopolymers Prepared by Alternating Ring-Opening Metathesis Polymerization Provide Access to Distinct, Multivalent Structures for the Probing of Biological Activity Open
A myriad of biological processes are facilitated by ligand-receptor interactions. The low affinities of these interactions are typically enhanced by multivalent engagements to promote binding. However, each biological interaction requires …
View article: Triblock Glycopolymers with Two 10-mer Blocks of Activating Sugars Enhance the Activation of Acrosomal Exocytosis in Mouse Sperm
Triblock Glycopolymers with Two 10-mer Blocks of Activating Sugars Enhance the Activation of Acrosomal Exocytosis in Mouse Sperm Open
Carbohydrate recognition is imperative for the induction of sperm acrosomal exocytosis (AE), an essential phenomenon in mammalian fertilization. In mouse sperm, polynorbornene 100-mers displaying fucose or mannose moieties were effective a…
View article: Uncovering the roles of <i>Mycobacterium tuberculosis melH</i> in redox and bioenergetic homeostasis: implications for antitubercular therapy
Uncovering the roles of <i>Mycobacterium tuberculosis melH</i> in redox and bioenergetic homeostasis: implications for antitubercular therapy Open
Mycobacterium tuberculosis ( Mtb ), the pathogenic bacterium that causes tuberculosis, has evolved sophisticated defense mechanisms to counteract the cytotoxicity of reactive oxygen species (ROS) generated within host macrophages during in…
View article: Glycopolymers Prepared by Alternating Ring-Opening Metathesis Polymerization Provide Access to Distinct, Multivalent Structures for the Probing of Biological Activity
Glycopolymers Prepared by Alternating Ring-Opening Metathesis Polymerization Provide Access to Distinct, Multivalent Structures for the Probing of Biological Activity Open
A myriad of biological processes are facilitated by ligand-receptor interactions. The low affinities of these interactions are typically enhanced by multivalent engagements to promote binding. However, each biological interaction requires …
View article: Uncovering the Roles of<i>Mycobacterium tuberculosis melH</i>in Redox and Bioenergetic Homeostasis: Implications for Antitubercular Therapy
Uncovering the Roles of<i>Mycobacterium tuberculosis melH</i>in Redox and Bioenergetic Homeostasis: Implications for Antitubercular Therapy Open
Mycobacterium tuberculosis ( Mtb ), the pathogenic bacterium that causes tuberculosis, has evolved sophisticated defense mechanisms to counteract the cytotoxicity of reactive oxygen species (ROS) generated within host macrophages during in…
View article: A Chemoproteomic Approach to Elucidate the Mechanism of Action of 6-Azasteroids with Unique Activity in Mycobacteria
A Chemoproteomic Approach to Elucidate the Mechanism of Action of 6-Azasteroids with Unique Activity in Mycobacteria Open
By illuminating key 6-azasteroid-protein interactions in both Mycobacterium tuberculosis (Mtb) and the closely related model organism Mycobacterium marinum (Mm), we sought to improve the antimycobacterial potency of 6-azasteroids and furth…
View article: Long-Range Kinetic Effects on the Alternating Ring Opening Metathesis of Bicyclo[4.2.0]oct-6-ene-7-carboxamides and Cyclohexene
Long-Range Kinetic Effects on the Alternating Ring Opening Metathesis of Bicyclo[4.2.0]oct-6-ene-7-carboxamides and Cyclohexene Open
We report an investigation of rates of ruthenium-catalyzed alternating ring opening metathesis (AROM) of cyclohexene with two different Ru-cyclohexylidene carbenes derived from bicyclo[4.2.0]oct-6-ene-7-carboxamides (A monomer) that bear d…
View article: Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Data from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Data from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Lack of target specificity by existing matrix metalloproteinase (MMP) inhibitors has hindered antimetastatic cancer drug discovery. Inhibitors that bind to noncatalytic sites of MMPs and disrupt protease signaling function have the potenti…
View article: Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Figure 1 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Methods, Figure Legends 1-3, Tables 1-2 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Data from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Data from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Lack of target specificity by existing matrix metalloproteinase (MMP) inhibitors has hindered antimetastatic cancer drug discovery. Inhibitors that bind to noncatalytic sites of MMPs and disrupt protease signaling function have the potenti…
View article: Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 Open
Supplementary Figures 2-3 from Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9
View article: Controlling Rheology of Fluid Interfaces through Microblock Length of Sequence‐Controlled Amphiphilic Copolymers
Controlling Rheology of Fluid Interfaces through Microblock Length of Sequence‐Controlled Amphiphilic Copolymers Open
Article 2200110 by Surita R. Bhatia and co-workers explores the rheology of fluid interfaces with sequence-specific amphiphilic copolymers. Copolymers contain short “microblocks” of 1–6 hydrophobic or hydrophilic repeat units. Results demo…
View article: Controlling Rheology of Fluid Interfaces through Microblock Length of Sequence‐Controlled Amphiphilic Copolymers
Controlling Rheology of Fluid Interfaces through Microblock Length of Sequence‐Controlled Amphiphilic Copolymers Open
Previous studies have demonstrated that films of sequence‐controlled amphiphilic copolymers display contact angles that depend on microblock size. This suggests that microblock length may provide a means of tuning surface and interfacial p…
View article: Corrigendum: Reductive Power Generated by Mycobacterium leprae Through Cholesterol Oxidation Contributes to Lipid and ATP Synthesis
Corrigendum: Reductive Power Generated by Mycobacterium leprae Through Cholesterol Oxidation Contributes to Lipid and ATP Synthesis Open
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View article: Substituent Effects Provide Access to Tetrasubstituted Ring-Opening Olefin Metathesis of Bicyclo[4.2.0]oct-6-enes
Substituent Effects Provide Access to Tetrasubstituted Ring-Opening Olefin Metathesis of Bicyclo[4.2.0]oct-6-enes Open
Herein, we report the origin of unexpected reactivity of bicyclo[4.2.0]oct-6-ene substrates containing an α,β-unsaturated amide moiety in ruthenium-catalyzed alternating ring-opening metathesis polymerization reactions. Specifically, compa…
View article: Reductive Power Generated by Mycobacterium leprae Through Cholesterol Oxidation Contributes to Lipid and ATP Synthesis
Reductive Power Generated by Mycobacterium leprae Through Cholesterol Oxidation Contributes to Lipid and ATP Synthesis Open
Upon infection, Mycobacterium leprae , an obligate intracellular bacillus, induces accumulation of cholesterol-enriched lipid droplets (LDs) in Schwann cells (SCs). LDs are promptly recruited to M. leprae -containing phagosomes, and inhibi…
View article: Enzymatic β-Oxidation of the Cholesterol Side Chain in <i>Mycobacterium tuberculosis</i> Bifurcates Stereospecifically at Hydration of 3-Oxo-cholest-4,22-dien-24-oyl-CoA
Enzymatic β-Oxidation of the Cholesterol Side Chain in <i>Mycobacterium tuberculosis</i> Bifurcates Stereospecifically at Hydration of 3-Oxo-cholest-4,22-dien-24-oyl-CoA Open
The unique ability of Mycobacterium tuberculosis (Mtb) to utilize host lipids such as cholesterol for survival, persistence, and virulence has made the metabolic pathway of cholesterol an area of great interest for therapeutics development…
View article: Retrospective feasibility study of <i>Mycobacterium tuberculosis</i> modified lipoprotein as a potential biomarker for TB detection in children
Retrospective feasibility study of <i>Mycobacterium tuberculosis</i> modified lipoprotein as a potential biomarker for TB detection in children Open
Background Current TB diagnostic methods available have been developed for adults and development efforts have neglected the differences in disease and sampling that occur between adults and children. Diagnostic challenges are even greater…
View article: Enzymatic β-Oxidation of the Cholesterol Side Chain in Mycobacterium Tuberculosis Bifurcates Stereospecifically at Hydration of 3-Oxo-Cholest-4,22- Dien-24-Oyl-CoA
Enzymatic β-Oxidation of the Cholesterol Side Chain in Mycobacterium Tuberculosis Bifurcates Stereospecifically at Hydration of 3-Oxo-Cholest-4,22- Dien-24-Oyl-CoA Open
The unique ability of Mycobacterium tuberculosis (Mtb) to utilize host lipids such as cholesterol for survival, persistence, and virulence has made the metabolic pathway of cholesterol an area of great interest for therapeutics development…
View article: Enzymatic β-Oxidation of the Cholesterol Side Chain in Mycobacterium Tuberculosis Bifurcates Stereospecifically at Hydration of 3-Oxo-Cholest-4,22- Dien-24-Oyl-CoA
Enzymatic β-Oxidation of the Cholesterol Side Chain in Mycobacterium Tuberculosis Bifurcates Stereospecifically at Hydration of 3-Oxo-Cholest-4,22- Dien-24-Oyl-CoA Open
The unique ability of Mycobacterium tuberculosis (Mtb) to utilize host lipids such as cholesterol for survival, persistence, and virulence has made the metabolic pathway of cholesterol an area of great interest for therapeutics development…
View article: Gradient copolymer prepared from alternating ring-opening metathesis of three monomers
Gradient copolymer prepared from alternating ring-opening metathesis of three monomers Open
A binary gradient copolymer in which the gradient is comprised of two copolymer dyads (1a-alt-2 and 1b-alt-2) is formed by metathesis of two different strained bicyclo[4.2.0]-amides (1a and 1b) and an unstrained cyclohexene monomer (2).
View article: The pursuit of mechanism of action: uncovering drug complexity in TB drug discovery
The pursuit of mechanism of action: uncovering drug complexity in TB drug discovery Open
The tools that have been successfully employed to understand the mechanism of action of TB therapeutics are discussed to offer insights into the future of mechanistic assessment in M. tuberculosis.